Display options
Cite
Galaev IY, Mattiasson B. Affinity thermoprecipitatin: Contribution of the efficiency of ligand-protein interaction and access of the ligand. Biotechnol Bioeng. 1993;41(11):1101-6doi: 10.1002/bit.260411113.
Galaev, I. Y., & Mattiasson, B. (1993). Affinity thermoprecipitatin: Contribution of the efficiency of ligand-protein interaction and access of the ligand. Biotechnology and bioengineering, 41(11), 1101-6. https://doi.org/10.1002/bit.260411113
Galaev, I Y, and Mattiasson, B. "Affinity thermoprecipitatin: Contribution of the efficiency of ligand-protein interaction and access of the ligand." Biotechnology and bioengineering vol. 41,11 (1993): 1101-6. doi: https://doi.org/10.1002/bit.260411113
Galaev IY, Mattiasson B. Affinity thermoprecipitatin: Contribution of the efficiency of ligand-protein interaction and access of the ligand. Biotechnol Bioeng. 1993 May;41(11):1101-6. doi: 10.1002/bit.260411113. PMID: 18601296.
Copy Download .nbib Format: NLM
Share it on

Biotechnol Bioeng. 1993 May;41(11):1101-6. doi: 10.1002/bit.260411113.

Affinity thermoprecipitatin: Contribution of the efficiency of ligand-protein interaction and access of the ligand.

Biotechnology and bioengineering

I Y Galaev, B Mattiasson

Affiliations

  1. Department of Biotechnology, Chemical Center, Lund University, PO Box 124, S-221 00 Lund, Sweden.

PMID: 18601296 DOI: 10.1002/bit.260411113

Abstract

Conjugates to two thermoprecipitating polymers, poly(N-vinyl caprolactam) and poly(N-isopropylacrylmide), with soybean trypsin inhibitor, Cibacron Blue 3GA, Cu-iminodiacetic acid, and p-aminobenzamidine were synthesized. The interaction of these conjugates with trypsin and lactate dehydrogenase was studied. Coupling of the ligand to a polymer resulted in a 100-1000-fold decrease in enzyme-affinity. Rough theoretical estimates revealed that a successful affinity precipitation required that the binding of a target protein and a ligand coupled to a polymer have binding constants on the order of 10(-7)-10(-8) M. Such strong affinity of low molecular weight ligands that can provide binding constants of 10(-9)-10(-11) M or alternatively multipoint attachment of the target protein molecule. The ligand in the ligand-polymer conjugate is still accessible to the protein after thermoprecipitation, and the latter can bind with the particle of the dispersion of thermoprecipitated ligand-polymer precipitate may result in stripping of enzyme molecules from the surface of the particles.

Publication Types